ATP2A3

ATP2A3
Identifiers
Aliases	ATP2A3, SERCA3, ATPase sarcoplasmic/endoplasmic reticulum Ca2+ transporting 3
External IDs	OMIM: 601929; MGI: 1194503; HomoloGene: 69131; GeneCards: ATP2A3; OMA:ATP2A3 - orthologs
Gene location (Human) Chr. Chromosome 17 (human) Band 17p13.2 Start 3,923,870 bp End 3,964,464 bp
Gene location (Mouse) Chr. Chromosome 11 (mouse) Band 11|11 B4 Start 72,851,995 bp End 72,883,870 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in granulocyte olfactory zone of nasal mucosa spleen mucosa of transverse colon thymus lymph node blood bone marrow cells beta cell appendix Top expressed in submandibular gland parotid gland granulocyte islet of Langerhans pyloric antrum crypt of lieberkuhn of small intestine colon left colon thymus tibiofemoral joint More reference expression data BioGPS More reference expression data
Gene ontology Molecular function nucleotide binding P-type calcium transporter activity metal ion binding hydrolase activity ATP binding P-type proton-exporting transporter activity Cellular component integral component of membrane nuclear membrane endoplasmic reticulum membrane membrane sarcoplasmic reticulum platelet dense tubular network membrane endoplasmic reticulum nucleus sarcoplasmic reticulum membrane Biological process regulation of cardiac conduction ion transport ion transmembrane transport calcium ion transmembrane transport calcium ion transport cellular calcium ion homeostasis proton transmembrane transport Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 489 53313 Ensembl ENSG00000074370 ENSMUSG00000020788 UniProt Q93084 Q64518 RefSeq (mRNA) NM_005173 NM_174953 NM_174954 NM_174955 NM_174956 NM_174957 NM_174958 NM_001163336 NM_001163337 NM_016745 RefSeq (protein) NP_005164 NP_777613 NP_777614 NP_777615 NP_777616 NP_777617 NP_777618 NP_001156808 NP_001156809 NP_058025 Location (UCSC) Chr 17: 3.92 – 3.96 Mb Chr 11: 72.85 – 72.88 Mb PubMed search
Wikidata
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Sarcoplasmic/endoplasmic reticulum calcium ATPase 3 is an enzyme that in humans is encoded by the ATP2A3 gene.

This gene encodes one of the SERCA Ca²⁺-ATPases, which are intracellular pumps located in the sarcoplasmic or endoplasmic reticula of cells. SERCA3 expression was originally described as non-muscular, but was recently observed in cardiomyocyte. This enzyme catalyzes the hydrolysis of ATP coupled with the translocation of calcium from the cytosol to the sarcoplasmic reticulum lumen, and is involved in calcium sequestration associated with muscular excitation and contraction. Alternative splicing results in 6 transcript variants encoding different isoforms named SERCA3a to SERCA3f.

Cancer

ATP2A3 gene has been observed progressively downregulated in Human papillomavirus-positive neoplastic keratinocytes derived from uterine cervical preneoplastic lesions at different levels of malignancy. For this reason, ATP2A3 is likely to be associated with tumorigenesis and may be a potential prognostic marker for uterine cervical preneoplastic lesions progression.

External links

• Human ATP2A3 genome location and ATP2A3 gene details page in the UCSC Genome Browser.

Further reading

• Wuytack F, Papp B, Verboomen H, et al. (1994). "A sarco/endoplasmic reticulum Ca²⁺-ATPase 3-type Ca²⁺ pump is expressed in platelets, in lymphoid cells, and in mast cells". J. Biol. Chem. 269 (2): 1410–6. doi:10.1016/S0021-9258(17)42273-3. PMID 8288608.
• Dode L, De Greef C, Mountain I, et al. (1998). "Structure of the human sarco/endoplasmic reticulum Ca²⁺-ATPase 3 gene. Promoter analysis and alternative splicing of the SERCA3 pre-mRNA". J. Biol. Chem. 273 (22): 13982–94. doi:10.1074/jbc.273.22.13982. PMID 9593748.
• Poch E, Leach S, Snape S, et al. (1999). "Functional characterization of alternatively spliced human SERCA3 transcripts". Am. J. Physiol. 275 (6 Pt 1): C1449–58. doi:10.1152/ajpcell.1998.275.6.C1449. PMID 9843705.
• Martin V, Bredoux R, Corvazier E, et al. (2002). "Three novel sarco/endoplasmic reticulum Ca²⁺-ATPase (SERCA) 3 isoforms. Expression, regulation, and function of the membranes of the SERCA3 family". J. Biol. Chem. 277 (27): 24442–52. doi:10.1074/jbc.M202011200. PMID 11956212.
• Gélébart P, Kovács T, Brouland JP, et al. (2002). "Expression of endomembrane calcium pumps in colon and gastric cancer cells. Induction of SERCA3 expression during differentiation". J. Biol. Chem. 277 (29): 26310–20. doi:10.1074/jbc.M201747200. PMID 11986315.
• Dode L, Vilsen B, Van Baelen K, et al. (2003). "Dissection of the functional differences between sarco(endo)plasmic reticulum Ca²⁺-ATPase (SERCA) 1 and 3 isoforms by steady-state and transient kinetic analyses". J. Biol. Chem. 277 (47): 45579–91. doi:10.1074/jbc.M207778200. PMID 12207029.
• Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• Houston R (2003). "Longitudinal sections of unfixed muscle". Biotechnic & Histochemistry. 77 (4): 229–30. PMID 12503734.
• Borge PD, Wolf BA (2003). "Insulin receptor substrate 1 regulation of sarco-endoplasmic reticulum calcium ATPase 3 in insulin-secreting beta-cells". J. Biol. Chem. 278 (13): 11359–68. doi:10.1074/jbc.M209521200. PMID 12524443.
• Chandrasekera CP, Lytton J (2003). "Inhibition of human SERCA3 by PL/IM430. Molecular analysis of the interaction". J. Biol. Chem. 278 (14): 12482–8. doi:10.1074/jbc.M212745200. PMID 12540840.
• Gevaert K, Goethals M, Martens L, et al. (2004). "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides". Nat. Biotechnol. 21 (5): 566–9. doi:10.1038/nbt810. PMID 12665801. S2CID 23783563.
• Bobe R, Bredoux R, Corvazier E, et al. (2004). "Identification, expression, function, and localization of a novel (sixth) isoform of the human sarco/endoplasmic reticulum Ca²⁺ATPase 3 gene". J. Biol. Chem. 279 (23): 24297–306. doi:10.1074/jbc.M314286200. PMID 15028735.
• Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
• Brouland JP, Gélébart P, Kovàcs T, et al. (2005). "The loss of sarco/endoplasmic reticulum calcium transport ATPase 3 expression is an early event during the multistep process of colon carcinogenesis". Am. J. Pathol. 167 (1): 233–42. doi:10.1016/S0002-9440(10)62968-9. PMC 1603437. PMID 15972967.
• Hadri L, Pavoine C, Lipskaia L, et al. (2006). "Transcription of the sarcoplasmic/endoplasmic reticulum Ca²⁺-ATPase type 3 gene, ATP2A3, is regulated by the calcineurin/NFAT pathway in endothelial cells". Biochem. J. 394 (Pt 1): 27–33. doi:10.1042/BJ20051387. PMC 1385999. PMID 16250893.
• Wootton LL, Michelangeli F (2006). "The effects of the phenylalanine 256 to valine mutation on the sensitivity of sarcoplasmic/endoplasmic reticulum Ca²⁺ ATPase (SERCA) Ca²⁺ pump isoforms 1, 2, and 3 to thapsigargin and other inhibitors". J. Biol. Chem. 281 (11): 6970–6. doi:10.1074/jbc.M510978200. PMID 16410239.
• Chaâbane C, Corvazier E, Bredoux R, et al. (2006). "Sarco/endoplasmic reticulum Ca²⁺ATPase type 3 isoforms (SERCA3b and SERCA3f): distinct roles in cell adhesion and ER stress". Biochem. Biophys. Res. Commun. 345 (4): 1377–85. doi:10.1016/j.bbrc.2006.05.054. PMID 16725111.
• Bredoux R, Corvazier E, Dally S, et al. (2006). "Human platelet Ca²⁺-ATPases: new markers of cell differentiation as illustrated in idiopathic scoliosis". Platelets. 17 (6): 421–33. doi:10.1080/09537100600758719. PMID 16973504. S2CID 24473757.
• Ewing RM, Chu P, Elisma F, et al. (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry". Mol. Syst. Biol. 3 (1): 89. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931.